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Significance of the pathogenic mutation T372R in the Yin Yang 1 protein interaction with DNA – thermodynamic studies
Author(s) -
Nieborak Anna,
Górecki Andrzej
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12106
Subject(s) - missense mutation , zinc finger , mutation , dna , entropy (arrow of time) , chemistry , biology , microbiology and biotechnology , genetics , transcription factor , physics , gene , thermodynamics
This work focuses on the pathogenic missense mutation in YY 1 protein correlated with insulinomas. Based on in vitro studies, we demonstrate that the mutation does not affect the secondary structure of either zinc fingers or the N‐terminal fragment (NTF) of the protein. Apart from a slight increase in the protein's compactness, no changes in the tertiary structure were observed. The introduced mutation significantly alters DNA ‐binding properties, both the affinity and enthalpy‐entropy contribution of the process, which are highly dependent on the recognized sequence. Obtained results indicate concerted rather than a modular mode of sequence recognition by YY 1 with the significant impact of a disordered NTF.